ZFYV1_PONAB
ID ZFYV1_PONAB Reviewed; 789 AA.
AC Q5RFL4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Zinc finger FYVE domain-containing protein 1;
GN Name=ZFYVE1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the formation of lipid droplets (LDs) which
CC are storage organelles at the center of lipid and energy homeostasis
CC (By similarity). Regulates the morphology, size and distribution of LDs
CC (By similarity). Mediates the formation of endoplasmic reticulum-lipid
CC droplets (ER-LD) contact sites by forming a complex with RAB18 and ZW10
CC (By similarity). Binds to phosphatidylinositol 3-phosphate (PtdIns3P)
CC through FYVE-type zinc finger (By similarity).
CC {ECO:0000250|UniProtKB:Q9HBF4}.
CC -!- SUBUNIT: Interacts with RAB18 (in GTP-bound form) (By similarity).
CC Interacts with BSCL2 in a RAB18-dependent manner (By similarity).
CC Interacts with ZW10 (By similarity). {ECO:0000250|UniProtKB:Q9HBF4}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q9HBF4}.
CC Golgi apparatus, Golgi stack {ECO:0000250|UniProtKB:Q9HBF4}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9HBF4}. Preautophagosomal
CC structure {ECO:0000250|UniProtKB:Q9HBF4}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q9HBF4}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9HBF4}. Note=Resides predominantly in the
CC cisternal stacks of the Golgi. Colocalizes with TRIM13 on the
CC perinuclear endoplasmic reticulum. During starvation conditions,
CC localizes to omegasomes which are endoplasmic reticulum connected
CC strutures at the origin of preautophagosomal structures. Localizes to
CC lipid droplets in the presence of oleic acid (By similarity).
CC {ECO:0000250|UniProtKB:Q9HBF4}.
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DR EMBL; CR857141; CAH89443.1; -; mRNA.
DR RefSeq; NP_001124616.1; NM_001131144.2.
DR AlphaFoldDB; Q5RFL4; -.
DR STRING; 9601.ENSPPYP00000006780; -.
DR GeneID; 100171453; -.
DR KEGG; pon:100171453; -.
DR CTD; 53349; -.
DR eggNOG; KOG1818; Eukaryota.
DR InParanoid; Q5RFL4; -.
DR OrthoDB; 198211at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:1990462; C:omegasome; ISS:UniProtKB.
DR GO; GO:0000407; C:phagophore assembly site; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR042427; ZFYV1.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46624; PTHR46624; 1.
DR Pfam; PF01363; FYVE; 2.
DR SMART; SM00064; FYVE; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS50178; ZF_FYVE; 2.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Golgi apparatus; Lipid droplet; Metal-binding;
KW Mitochondrion; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..789
FT /note="Zinc finger FYVE domain-containing protein 1"
FT /id="PRO_0000357049"
FT ZN_FING 598..659
FT /note="FYVE-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT ZN_FING 715..775
FT /note="FYVE-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 416..788
FT /note="Required for localization in the lipid droplets"
FT /evidence="ECO:0000250|UniProtKB:Q9HBF4"
FT BINDING 604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 607
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 620
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 623
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 628
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 631
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 651
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 654
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 721
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 724
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 737
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 740
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 745
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 748
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 767
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 770
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 789 AA; 88298 MW; D09D929580C962B6 CRC64;
MSAQTSPAEK GLNPGLMCQE SYACSGTDEA IFECDECCSL QCLRCEEELH RQERLRNHER
IRLKPGHVPY CDLCKGLSGH LPGVRQRAIV RCQTCKINLC LECQKRTHSG GNKRRHPVTV
YNVSNLQESL EAEEMDEETK RKKMTEKVVS FLLVDENEEI QVTNEEDFIR KLDCKPDQHL
KVASIFGNTG DGKSHTLNHT FFYGREVFKT SPTQESCTVG VWAAYDPVHK VAVIDTEGLL
GATVNLSQRT RLLLKVLAIS DLVIYRTHAD RLHNDLFKFL GDASEAYLKH YTKELKATTA
RCGLDVPLST LGPAVIIFHE TVHTQLLGSD HPSEVPEKLI QDRFRKLGRF PEAFSSIHYK
GTRTYNPPTD FSGLRRALEQ LLENNTTRSP RHPGVIFKAL KALSDRFSGE IPDDQMAHSS
FFPDEYFTCS SLCLSCGVGC KNSMNHGKEG VPHEAKSRCR YSHQYDNRVY TCKACYEGGE
EVSVVPKTSA STDSPWMGLA KYAWSGYVIE CPNCGVVYRS RQYWFGNQDP VDTVVRTEIV
HVWPGTDGFL KDNNNAAQRL LDGMNFMAQS VSELSLGPTK AVTSWLTDQI APAYWRPNSQ
ILSCNKCATS FKDNDTKHHC RACGEGFCDS CSSKTRPVPE RGWGPAPVRV CDNCYEARNV
QLAVTEAQVD DEGGTLIARK VGEAVQNTLG AVVTAIDIPL GLVKDAARPA YWVPDHEILH
CHNCRKEFSI KLSKHHCRAC GQGFCDECSH DRRAVPSRGW DHPVRVCFNC NKKPAWTSLS
VMTGKGPLC
